NDLI: Characterization of two alkyl hydroperoxide reductase C homologs alkyl hydroperoxide reductase C_H1 and alkyl hydroperoxide reductase C

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Characterization of two alkyl hydroperoxide reductase C homologs alkyl hydroperoxide reductase C_H1 and alkyl hydroperoxide reductase C_H2 in Bacillus subtilis.

Content Provider	Europe PMC
Author	Cha, Mee-Kyung Bae, Yoo-Jeen Kim, Kyu-Jeong Park, Byung-Joon Kim, Il-Han
Copyright Year	2015
Abstract	AIM: To identify alkyl hydroperoxide reductase subunit C (AhpC) homologs in Bacillus subtilis (B. subtilis) and to characterize their structural and biochemical properties. AhpC is responsible for the detoxification of reactive oxygen species in bacteria. METHODS: Two AhpC homologs (AhpC_H1 and AhpC_H2) were identified by searching the B. subtilis database; these were then cloned and expressed in Escherichia coli. AhpC mutants carrying substitutions of catalytically important Cys residues (C37S, C47S, C166S, C37/47S, C37/166S, C47/166S, and C37/47/166S for AhpC_H1; C52S, C169S, and C52/169S for AhpC_H2) were obtained by site-directed mutagenesis and purified, and their structure-function relationship was analyzed. The B. subtilis ahpC genes were disrupted by the short flanking homology method, and the phenotypes of the resulting AhpC-deficient bacteria were examined. RESULTS: Comparative characterization of AhpC homologs indicates that AhpC_H1 contains an extra C37, which forms a disulfide bond with the peroxidatic C47, and behaves like an atypical 2-Cys AhpC, while AhpC_H2 functions like a typical 2-Cys AhpC. Tryptic digestion analysis demonstrated the presence of intramolecular Cys37-Cys47 linkage, which could be reduced by thioredoxin, resulting in the association of the dimer into higher-molecular-mass complexes. Peroxidase activity analysis of Cys→Ser mutants indicated that three Cys residues were involved in the catalysis. AhpC_H1 was resistant to inactivation by peroxide substrates, but had lower activity at physiological H2O2 concentrations compared to AhpC_H2, suggesting that in B. subtilis, the enzymes may be physiologically functional at different substrate concentrations. The exposure to organic peroxides induced AhpC_H1 expression, while AhpC_H1-deficient mutants exhibited growth retardation in the stationary phase, suggesting the role of AhpC_H1 as an antioxidant scavenger of lipid hydroperoxides and a stress-response factor in B. subtilis. CONCLUSION: AhpC_H1, a novel atypical 2-Cys AhpC, is functionally distinct from AhpC_H2, a typical 2-Cys AhpC.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC4549766&blobtype=pdf
ISSN	19498454
Volume Number	6
DOI	10.4331/wjbc.v6.i3.249
PubMed Central reference number	PMC4549766
Issue Number	3
PubMed reference number	26322180
Journal	World Journal of Biological Chemistry [World J Biol Chem]
e-ISSN	19498454
Language	English
Publisher	Baishideng Publishing Group Inc
Publisher Date	2015-08-01
Access Restriction	Open
Rights License	©The Author(s) 2015. Published by Baishideng Publishing Group Inc. All rights reserved.
Subject Keyword	Cysteine-dependent peroxidase Thioredoxin Thiol peroxidase Peroxiredoxin Alkyl hydroperoxide Ortholog Bacillus subtilis Oxidative stress
Content Type	Text
Resource Type	Article
Subject	Biochemistry (medical)

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